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Wiley, FEBS Letters, 2(152), p. 300-304

DOI: 10.1016/0014-5793(83)80400-1

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The complete amino acid sequence of the bifunctional α-amylase/trypsin inhibitor from seeds of ragi (Indian finger millet,Eleusine coracanaGaertn.)

Journal article published in 1983 by F. A. P. Campos ORCID, M. Richardson
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The complete amino acid sequence of the bifunctional α-amylase/trypsin inhibitor from ragi seeds was determined by analysis of fragments and peptides derived from the protein by cleavage with cyanogen bromide and by digestion with trypsin, chymotrypsin, thermolysin, the S. aureus V8 protease and a Pro-specific protease. The molecular consists of a single polypeptide chain of 122 amino acids which exhibits sequence homology with trypsin inhibitors from barley and maize and with an α-amylase inhibitor from wheat.